FOOD SCIENCE ›› 2019, Vol. 40 ›› Issue (20): 87-93.doi: 10.7506/spkx1002-6630-20180831-367

• Food Chemistry • Previous Articles     Next Articles

SUN Qian, ZHANG Aiqin, XUE Yufei, CAO Wenli, XI Fengling, WANG Ronghao, LI Fang, KONG Lingming

SUN Qian, ZHANG Aiqin, XUE Yufei, CAO Wenli, XI Fengling, WANG Ronghao, LI Fang, KONG Lingming   

  1. (1. College of Food and Pharmaceutics, Xinjiang Agricultural University, ürümqi 830052, China;2. Xinjiang Institute of Light Technology, ürümqi 830021, China)
  • Online:2019-10-25 Published:2019-10-25

Abstract: Walnut glutenin, constituting up to more than 70% of the total proteins in walnut, was modified chemically (acylated or phosphorylated). After acylation or phosphorylation, the solubility of the glutenin was increased by 4.61 and 5.49 times, and the water-holding capacity by 2.97 and 2.55 times, respectively. The oil-holding capacity was slightly reduced, and the emulsifying capacity and foaming capacity were not changed substantially. Spectroscopic analyses showed that both the secondary and tertiary structures of the protein were changed, leading to changes in the functional properties of the protein. This study provides useful information for further analysis of the changes in functional properties of walnut glutenin.

Key words: walnut glutenin, chemical modification, spectroscopic analysis, scanning electron microscopy

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